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Matrix Remodeling During Endochondral Ossification

Overview
Specialty Cell Biology
Date 2004 Apr 23
PMID 15102440
Citations 155
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Abstract

Endochondral ossification, the process by which most of the skeleton is formed, is a powerful system for studying various aspects of the biological response to degraded extracellular matrix (ECM). In addition, the dependence of endochondral ossification upon neovascularization and continuous ECM remodeling provides a good model for studying the role of the matrix metalloproteases (MMPs) not only as simple effectors of ECM degradation but also as regulators of active signal-inducers for the initiation of endochondral ossification. The daunting task of elucidating their specific role during endochondral ossification has been facilitated by the development of mice deficient for various members of this family. Here, we discuss the ECM and its remodeling as one level of molecular regulation for the process of endochondral ossification, with special attention to the MMPs.

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References
1.
Van Wart H, Birkedal-Hansen H . The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc Natl Acad Sci U S A. 1990; 87(14):5578-82. PMC: 54368. DOI: 10.1073/pnas.87.14.5578. View

2.
Flenniken A, Williams B . Developmental expression of the endogenous TIMP gene and a TIMP-lacZ fusion gene in transgenic mice. Genes Dev. 1990; 4(7):1094-106. DOI: 10.1101/gad.4.7.1094. View

3.
Reponen P, Sahlberg C, Munaut C, Thesleff I, Tryggvason K . High expression of 92-kD type IV collagenase (gelatinase B) in the osteoclast lineage during mouse development. J Cell Biol. 1994; 124(6):1091-1102. PMC: 2119973. DOI: 10.1083/jcb.124.6.1091. View

4.
Mattot V, Raes M, Henriet P, Eeckhout Y, Stehelin D, Vandenbunder B . Expression of interstitial collagenase is restricted to skeletal tissue during mouse embryogenesis. J Cell Sci. 1995; 108 ( Pt 2):529-35. DOI: 10.1242/jcs.108.2.529. View

5.
Gack S, Vallon R, Schmidt J, Grigoriadis A, Tuckermann J, Schenkel J . Expression of interstitial collagenase during skeletal development of the mouse is restricted to osteoblast-like cells and hypertrophic chondrocytes. Cell Growth Differ. 1995; 6(6):759-67. View